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@ARTICLE{Zhang:155577,
      author       = {Zhang, Zhengrong and Zheng, You and Niu, Zubiao and Zhang,
                      Bo and Wang, Chenxi and Yao, Xiaohong and Peng, Haoran and
                      Franca, Del Nonno and Wang, Yunyun and Zhu, Yichao and Su,
                      Yan and Tang, Meng and Jiang, Xiaoyi and Ren, He and He,
                      Meifang and Wang, Yuqi and Gao, Lihua and Zhao, Ping and
                      Shi, Hanping and Chen, Zhaolie and Wang, Xiaoning and
                      Piacentini, Mauro and Bian, Xiuwu and Melino, Gerry and Liu,
                      Liang and Huang, Hongyan and Sun, Qiang},
      title        = {{SARS}-{C}o{V}-2 spike protein dictates syncytium-mediated
                      lymphocyte elimination.},
      journal      = {Cell death and differentiation},
      volume       = {28},
      number       = {9},
      issn         = {1476-5403},
      address      = {London},
      publisher    = {Macmillan},
      reportid     = {DZNE-2021-00755},
      pages        = {2765-2777},
      year         = {2021},
      abstract     = {The severe acute respiratory syndrome coronavirus 2
                      (SARS-CoV-2) virus is highly contagious and causes
                      lymphocytopenia, but the underlying mechanisms are poorly
                      understood. We demonstrate here that heterotypic
                      cell-in-cell structures with lymphocytes inside
                      multinucleate syncytia are prevalent in the lung tissues of
                      coronavirus disease 2019 (COVID-19) patients. These unique
                      cellular structures are a direct result of SARS-CoV-2
                      infection, as the expression of the SARS-CoV-2 spike
                      glycoprotein is sufficient to induce a rapid (~45.1 nm/s)
                      membrane fusion to produce syncytium, which could readily
                      internalize multiple lines of lymphocytes to form typical
                      cell-in-cell structures, remarkably leading to the death of
                      internalized cells. This membrane fusion is dictated by a
                      bi-arginine motif within the polybasic S1/S2 cleavage site,
                      which is frequently present in the surface glycoprotein of
                      most highly contagious viruses. Moreover, candidate
                      anti-viral drugs could efficiently inhibit spike
                      glycoprotein processing, membrane fusion, and cell-in-cell
                      formation. Together, we delineate a molecular and cellular
                      rationale for SARS-CoV-2 pathogenesis and identify novel
                      targets for COVID-19 therapy.},
      keywords     = {COVID-19: pathology / COVID-19: virology / Cell Line / Cell
                      Line, Tumor / Giant Cells: pathology / Giant Cells: virology
                      / HEK293 Cells / HeLa Cells / Humans / Jurkat Cells / K562
                      Cells / Lymphocytes: pathology / Lymphocytes: virology /
                      SARS-CoV-2: metabolism / SARS-CoV-2: pathogenicity / Spike
                      Glycoprotein, Coronavirus: metabolism / Virus
                      Internalization / Virus Replication: genetics},
      cin          = {AG Nicotera},
      ddc          = {610},
      cid          = {I:(DE-2719)5000018},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33879858},
      pmc          = {pmc:PMC8056997},
      doi          = {10.1038/s41418-021-00782-3},
      url          = {https://pub.dzne.de/record/155577},
}